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dc.contributor.authorReimann, Frank
dc.contributor.authorDiakogiannaki, Eleftheria
dc.contributor.authorMoss, Catherine E
dc.contributor.authorGribble, Fiona M
dc.date.accessioned2019-11-21T00:30:51Z
dc.date.available2019-11-21T00:30:51Z
dc.date.issued2020-03
dc.identifier.issn0196-9781
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/299097
dc.description.abstractGlucose-dependent insulinotropic polypeptide (GIP) is a gut hormone secreted from the upper small intestine, which plays an important physiological role in the control of glucose metabolism through its incretin action to enhance glucose-dependent insulin secretion. GIP has also been implicated in postprandial lipid homeostasis. GIP is secreted from enteroendocrine K-cells residing in the intestinal epithelium. K-cells sense a variety of components found in the gut lumen following food consumption, resulting in an increase in plasma GIP signal dependent on the nature and quantity of ingested nutrients. We review the evidence for an important role of sodium-coupled glucose uptake through SGLT1 for carbohydrate sensing, of free-fatty acid receptors FFAR1/FFAR4 and the monoacyl-glycerol sensing receptor GPR119 for lipid detection, of the calcium-sensing receptor CASR and GPR142 for protein sensing, and additional modulation by neurotransmitters such as somatostatin and galanin. These pathways have been identified through combinations of in vivo, in vitro and molecular approaches.
dc.description.sponsorshipWellcome Trust BBSRC MRC
dc.format.mediumPrint-Electronic
dc.languageeng
dc.publisherElsevier BV
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectHumans
dc.subjectGastric Inhibitory Polypeptide
dc.subjectGlucose
dc.subjectReceptors, G-Protein-Coupled
dc.subjectReceptors, Calcium-Sensing
dc.subjectEnteroendocrine Cells
dc.subjectSodium-Glucose Transporter 1
dc.subjectInsulin Secretion
dc.titleCellular mechanisms governing glucose-dependent insulinotropic polypeptide secretion.
dc.typeArticle
prism.publicationDate2020
prism.publicationNamePeptides
prism.startingPage170206
prism.volume125
dc.identifier.doi10.17863/CAM.46159
dcterms.dateAccepted2019-11-14
rioxxterms.versionofrecord10.1016/j.peptides.2019.170206
rioxxterms.versionAM
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2020-03
dc.contributor.orcidReimann, Frank [0000-0001-9399-6377]
dc.contributor.orcidGribble, Fiona [0000-0002-4232-2898]
dc.identifier.eissn1873-5169
rioxxterms.typeJournal Article/Review
pubs.funder-project-idWellcome Trust (084210/Z/07/Z)
pubs.funder-project-idWellcome Trust (084210/Z/07/A)
pubs.funder-project-idMedical Research Council (MC_UU_12012/3)
pubs.funder-project-idWellcome Trust (106262/Z/14/Z)
pubs.funder-project-idMRC (MC_UU_00014/3)
pubs.funder-project-idMRC (MC_UU_00014/5)
cam.issuedOnline2019-11-19
cam.orpheus.successThu Jan 30 10:36:46 GMT 2020 - Embargo updated
rioxxterms.freetoread.startdate2020-11-19


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Attribution-NonCommercial-NoDerivatives 4.0 International
Except where otherwise noted, this item's licence is described as Attribution-NonCommercial-NoDerivatives 4.0 International